4NN0

Crystal structure of the C1QTNF5 globular domain in space group P63

Summary for 4NN0

• Entry DOI: 10.2210/pdb4nn0/pdb
• Related: 4F3J
• Descriptor: Complement C1q tumor necrosis factor-related protein 5, 1,2-ETHANEDIOL, SULFATE ION, ... (5 entities in total)
• Functional Keywords: l-ormd, late onset retinal macular degeneration, s163r, 10-strand jelly-roll fold, cellular adhesion, cell adhesion
• Biological source: Homo sapiens (human)
• Cellular location: Secreted (Probable): Q9BXJ0
• Total number of polymer chains: 3
• Total formula weight: 50796.40

Authors

Tu, X.,Palczewski, K. (deposition date: 2013-11-15, release date: 2014-03-26, Last modification date: 2023-09-20)

Primary citation

Tu, X.,Palczewski, K.
The macular degeneration-linked C1QTNF5 (S163) mutation causes higher-order structural rearrangements.
J.Struct.Biol., 186:86-94, 2014

PubMed Abstract: The C1q-tumor necrosis factor 5 (C1QTNF5) protein plays a significant role in retinal pigmented epithelium (RPE) cellular adhesion. The C1QTNF5 gene is co-transcribed with the frizzled-related protein (MFRP) gene. A Ser-to-Arg mutation at site 163 (S163R) in C1QTNF5 is known to cause late-onset retinal macular degeneration (L-ORMD). Here we also found that C1QTNF5 monomers can multimerize into a bouquet-like octadecamer. We found that a novel intermolecular hydrogen-bond network of S163 that glues adjacent globular heads of C1QTNF5 together was weakened or abolished by the R163 pathogenic mutation. These findings could underlie the structural basis of this protein's adhesive function and relate to the pathogenesis of its S163R mutation. Additionally, the fact that C1QTNF5 immobilized to a resin selectively enriched detergent extracted membrane-bound MFRP, further confirmed their interaction, implying functions other than cellular adhesion for C1QTNF5.

PubMed: 24531000
DOI: 10.1016/j.jsb.2014.02.001

Experimental method

X-RAY DIFFRACTION (1.42 Å)